1.8.4.11	L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O	-	-	
1.8.4.11	L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O	3-step ping pong reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview	658215	
1.8.4.11	L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O	3-step reaction mechanism involving catalytic and recycling cysteine residues, formation of a sulfenic acid reaction intermediate, overview	658215	
1.8.4.11	L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O	catalytic mechanism and structural features, roles of cysteine residues, active site structure	-, 658216	
1.8.4.11	L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O	catalytic mechanism involves the formation of a sulfenic acid intermediate	658214	
1.8.4.11	L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O	catalytic mechanism involving the formation of a sulfenic acid intermediate, Cys52 is involved	658212	
1.8.4.11	L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O	catalytic mechanism involving the formation of a sulfenic acid intermediate, Cys72, Cys218 and Cys228 are involved	658212	
1.8.4.11	L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O	catalytic mechanism of MsrA, active site structure, modeling of protein-bound methionine sulfoxide recognition and repair from the crystal structure	659028	
1.8.4.11	L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O	catalytic mechanism of MsrA, the rate limiting step occurs after formation of the sulfenic acid intermediate and is associated with either the Cys51/Cys198 disulfide bond formation or the thioredoxin reduction process	659275	
1.8.4.11	L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O	reaction mechanism	394110, 657641	
1.8.4.11	L-methionine (S)-sulfoxide + thioredoxin = L-methionine + thioredoxin disulfide + H2O	reaction mechanism, modeling of substrate binding at the active site, Cys72 is involved	659992	
1.8.4.11	L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin	proposed catalytic mechanism of the reductase step of MsrA	684715	
1.8.4.11	peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin	-	-	
1.8.4.11	peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin	catalytic mechanism, Cys72 is essential for activity forming disulfide bonds with either Cys218 or Cys227	394100	
1.8.4.11	peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin	catalytic mechanism, rate-limiting reduction of the Cys51-Cys198 disulfide bond by thioredoxin and formation of the thiosulfenic acid intermediate on Cys51	659275	
1.8.4.11	peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin	presence of at least two binding subsites. The first one, whose contribution is major in the efficiency of the reductase step and in which the epsilon-methyl group of MetSO binds, is the hydrophobic pocket formed by Phe52 and Trp53, the position of the indole ring being stabilized by interactions with His186 and Tyr189. The second subsite composed of Asp129 and Tyr197 contributes to the binding of the main chain of the substrate but to a lesser extent	687569